P56961 (ARODE_CHLMU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 87.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Shikimate biosynthesis protein AroDE | ||||||
| Gene names |
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| Organism | Chlamydia muridarum [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83560 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia |
Protein attributes
| Sequence length | 478 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Bifunctional enzyme that catalyzes two sequential steps of the aromatic amino acids biosynthetic pathway. The first reaction is catalyzed by the 3-dehydroquinate dehydratase, coded by the AroD domain; the second reaction is catalyzed by the shikimate 5-dehydrogenase, coded by the AroE domain. HAMAP MF_00214 |
| Catalytic activity | 3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00214 Shikimate + NADP+ = 3-dehydroshikimate + NADPH. HAMAP MF_00214 |
| Pathway | Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00214 |
| Sequence similarities | In the N-terminal section; belongs to the type-I 3-dehydroquinase family. In the C-terminal section; belongs to the shikimate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis |
| Ligand | NADP Schiff base |
| Molecular function | Lyase Oxidoreductase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: EC NADP bindingInferred from electronic annotation. Source: InterPro shikimate 3-dehydrogenase (NADP+) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 478 | 478 | Shikimate biosynthesis protein AroDE HAMAP MF_00214 | PRO_0000138822 | |||||
Regions | |||||||||
| Nucleotide binding | 337 – 341 | 5 | NADP By similarity | ||||||
| Region | 1 – 208 | 208 | 3-dehydroquinate dehydratase HAMAP MF_00214 | ||||||
| Region | 209 – 478 | 270 | Shikimate 5-dehydrogenase HAMAP MF_00214 | ||||||
Sites | |||||||||
| Active site | 110 | 1 | Proton acceptor By similarity | ||||||
| Active site | 133 | 1 | Schiff-base intermediate with substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. Fraser C.M.Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE002160 Genomic DNA. Translation: AAF39475.1. |
| PIR | G81679. |
| RefSeq | NP_297023.1. NC_002620.2. |
3D structure databases | |
| ProteinModelPortal | P56961. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1246010. |
| GenomeReviews | Gene locus TC_0649 in contig AE002160_GR. |
| KEGG | cmu:TC0649. |
| PATRIC | 20372752. VBIChlMur19118_0688. |
| TIGR | TC_0649. |
Phylogenomic databases | |
| HOGENOM | HBG414053. |
| OMA | ISHLSHN. |
| ProtClustDB | PRK09310. |
Enzyme and pathway databases | |
| BioCyc | CMUR243161:TC_0649-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00214. AroD. Fused. [Tree] MF_00222. Shikimate_DH_AroE. Fused. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR001381. DHquinase_I. IPR016040. NAD(P)-bd_dom. IPR011342. Shikimate_DH. IPR013708. Shikimate_DH-bd_N. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K13832. |
| Pfam | PF01487. DHquinase_I. 1 hit. PF01488. Shikimate_DH. 1 hit. PF08501. Shikimate_dh_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00507. AroE. 1 hit. |
| PROSITE | PS01028. DEHYDROQUINASE_I. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARODE_CHLMU | ||||||||
| Accession | Primary (citable) accession number: P56961 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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